UniProtKB - Q8U1N9 (MRE11_PYRFU)
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>sp|Q8U1N9|MRE11_PYRFU DNA double-strand break repair protein Mre11 OS=Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) OX=186497 GN=mre11 PE=1 SV=2 MKFAHLADIHLGYEQFHKPQREEEFAEAFKNALEIAVQENVDFILIAGDLFHSSRPSPGT LKKAIALLQIPKEHSIPVFAIEGNHDRTQRGPSVLNLLEDFGLVYVIGMRKEKVENEYLT SERLGNGEYLVKGVYKDLEIHGMKYMSSAWFEANKEILKRLFRPTDNAILMLHQGVREVS EARGEDYFEIGLGDLPEGYLYYALGHIHKRYETSYSGSPVVYPGSLERWDFGDYEVRYEW DGIKFKERYGVNKGFYIVEDFKPRFVEIKVRPFIDVKIKGSEEEIRKAIKRLIPLIPKNA YVRLNIGWRKPFDLTEIKELLNVEYLKIDTWRIKERTDEESGKIGLPSDFFTEFELKIID ILGEKDFDDFDYIIKLITEGKVEEEGPLEEAVKKVSEEKGKTVRQKIESIPKKKRGTLDS WLGGARCommunity curation ()Add a publicationFeedback
Protein
DNA double-strand break repair protein Mre11
Gene
mre11
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score:
Annotation score:5 out of 5
<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>Select a section on the left to see content.
<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni
Part of the Rad50/Mre11 complex, which is involved in the early steps of DNA double-strand break (DSB) repair (PubMed:11029422, PubMed:18854158, PubMed:18957200). The complex may facilitate opening of the processed DNA ends to aid in the recruitment of HerA and NurA (PubMed:18957200). Mre11 binds to DSB ends and has both double-stranded 3'-5' exonuclease activity and single-stranded endonuclease activity (PubMed:11029422, PubMed:18854158, PubMed:18957200).3 Publications
<p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More...</a></p> Manual assertion based on experiment ini
- Ref.2"Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine."
Hopfner K.-P., Karcher A., Shin D., Fairley C., Tainer J.A., Carney J.P.
J. Bacteriol. 182:6036-6041(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR. - Ref.3"The P. furiosus mre11/rad50 complex promotes 5' strand resection at a DNA double-strand break."
Hopkins B.B., Paull T.T.
Cell 135:250-260(2008) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION. - Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori
Mn2+
- Search proteins in UniProtKB for this molecule.
- Search chemical reactions in Rhea for this molecule.
- See the description of this molecule in ChEBI.
<p>Manual validated information which has been generated by the UniProtKB automatic annotation system.</p> <p><a href="/manual/evidences#ECO:0000255">More...</a></p> Manual assertion according to rulesi
5 PublicationsManual assertion based on experiment ini
- Ref.2"Mre11 and Rad50 from Pyrococcus furiosus: cloning and biochemical characterization reveal an evolutionarily conserved multiprotein machine."
Hopfner K.-P., Karcher A., Shin D., Fairley C., Tainer J.A., Carney J.P.
J. Bacteriol. 182:6036-6041(2000) [PubMed] [Europe PMC] [Abstract]Cited for: FUNCTION, COFACTOR. - Ref.6"Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase."
Hopfner K.-P., Karcher A., Craig L., Woo T.T., Carney J.P., Tainer J.A.
Cell 105:473-485(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-333 IN COMPLEX WITH MANGANESE, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.7"Structural and functional analysis of Mre11-3."
Arthur L.M., Gustausson K., Hopfner K.P., Carson C.T., Stracker T.H., Karcher A., Felton D., Weitzman M.D., Tainer J., Carney J.P.
Nucleic Acids Res. 32:1886-1893(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 OF MUTANT PFMRE11-3 IN COMPLEX WITH MANGANESE, COFACTOR, ACTIVE SITE. - Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97. - Ref.10"Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair."
Limbo O., Moiani D., Kertokalio A., Wyman C., Tainer J.A., Russell P.
Nucleic Acids Res. 40:11435-11449(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 OF MUTANT ARG-204 IN COMPLEX WITH MANGANESE, COFACTOR.
Manual assertion according to rulesi
4 PublicationsManual assertion based on experiment ini
- Ref.6"Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase."
Hopfner K.-P., Karcher A., Craig L., Woo T.T., Carney J.P., Tainer J.A.
Cell 105:473-485(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-333 IN COMPLEX WITH MANGANESE, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.7"Structural and functional analysis of Mre11-3."
Arthur L.M., Gustausson K., Hopfner K.P., Carson C.T., Stracker T.H., Karcher A., Felton D., Weitzman M.D., Tainer J., Carney J.P.
Nucleic Acids Res. 32:1886-1893(2004) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 OF MUTANT PFMRE11-3 IN COMPLEX WITH MANGANESE, COFACTOR, ACTIVE SITE. - Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97. - Ref.10"Mre11 ATLD17/18 mutation retains Tel1/ATM activity but blocks DNA double-strand break repair."
Limbo O., Moiani D., Kertokalio A., Wyman C., Tainer J.A., Russell P.
Nucleic Acids Res. 40:11435-11449(2012) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-333 OF MUTANT ARG-204 IN COMPLEX WITH MANGANESE, COFACTOR.
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi
Nuclease activity is regulated by Rad50.UniRule annotation
Manual assertion according to rulesi
2 PublicationsManual assertion based on experiment ini
- Ref.4"ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease."
Majka J., Alford B., Ausio J., Finn R.M., McMurray C.T.
J. Biol. Chem. 287:2328-2341(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, SUBUNIT. - Ref.5"ATP-driven Rad50 conformations regulate DNA tethering, end resection, and ATM checkpoint signaling."
Deshpande R.A., Williams G.J., Limbo O., Williams R.S., Kuhnlein J., Lee J.H., Classen S., Guenther G., Russell P., Tainer J.A., Paull T.T.
EMBO J. 33:482-500(2014) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION.
Sites
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi | 8 | Manganese 1Combined sources <p>Manually validated information inferred from a combination of experimental and computational evidence.</p> <p><a href="/manual/evidences#ECO:0007744">More...</a></p> Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 10 | Manganese 1; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 49 | Manganese 1Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 49 | Manganese 2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 84 | Manganese 2Combined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei | 85 | Proton donorUniRule annotation Manual assertion according to rulesi 2 Publications<p>Manually curated information which has been inferred by a curator based on his/her scientific knowledge or on the scientific content of an article.</p> <p><a href="/manual/evidences#ECO:0000305">More...</a></p> Manual assertion inferred by curator fromi
| 1 | |
| Metal bindingi | 173 | Manganese 2; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 206 | Manganese 2; via pros nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 | |
| Metal bindingi | 208 | Manganese 1; via tele nitrogenCombined sources Manual assertion inferred from combination of experimental and computational evidencei 4 PublicationsManual assertion based on experiment ini
| 1 |
<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni
- 3'-5' exonuclease activity Source: UniProtKB
<p>Inferred from Direct Assay</p>
<p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ida">GO evidence code guide</a></p>
Inferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
- DNA end binding Source: UniProtKBInferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
- endonuclease activity Source: UniProtKBInferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
- identical protein binding Source: IntAct
<p>Inferred from Physical Interaction</p>
<p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p>
<p>More information in the <a href="http://geneontology.org/page/guide%2Dgo%2Devidence%2Dcodes#ipi">GO evidence code guide</a></p>
Inferred from physical interactioni
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97. - "The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair."
Lammens K., Bemeleit D.J., Mockel C., Clausing E., Schele A., Hartung S., Schiller C.B., Lucas M., Angermuller C., Soding J., Strasser K., Hopfner K.P.
Cell 145:54-66(2011) [PubMed] [Europe PMC] [Abstract]
- manganese ion binding Source: UniProtKBInferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
- Y-form DNA binding Source: UniProtKBInferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
GO - Biological processi
- double-strand break repair Source: UniProtKBInferred from direct assayi
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97.
<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi
| Molecular function | Endonuclease, Exonuclease, Hydrolase, Nuclease |
| Biological process | DNA damage, DNA repair |
| Ligand | Manganese, Metal-binding |
<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi | Recommended name: DNA double-strand break repair protein Mre11UniRule annotationManual assertion according to rulesi Curated (EC:3.1.-.-
Manual assertion according to rulesi Curated)Alternative name(s): pfMre111 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More...</a></p> Manual assertion based on opinion ini
|
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi | Name:mre111 Publication Manual assertion based on opinion ini
Manual assertion according to rulesi Ordered Locus Names:PF1166 |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>Organismi | Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1) |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri | 186497 [NCBI] |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineagei | cellular organisms › Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › Pyrococcus furiosus |
| <p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi |
|
<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi
Mutagenesis
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi | 17 | H → A: Decreases 3'-5' exonuclease activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 52 | H → S: Lacks 3'-5' exonuclease activity. Slight decrease in endonuclease activity. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 61 | L → K: Decreases affinity for ssDNA and dsDNA, but does not affect exonuclease and endonuclease activities. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 85 | H → S: Lacks both 3'-5' exonuclease and endonuclease activities. 1 Publication Manual assertion based on experiment ini
| 1 | |
| Mutagenesisi | 97 | L → D: Decreases affinity for ssDNA and dsDNA, but does not affect exonuclease and endonuclease activities. 1 Publication Manual assertion based on experiment ini
| 1 |
<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi
Molecule processing
| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_0000138696 | 1 – 426 | DNA double-strand break repair protein Mre11Add BLAST | 426 |
<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni
<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei
Homodimer (PubMed:18854158).
Forms a heterotetramer composed of two Mre11 subunits and two Rad50 subunits (PubMed:11371344, PubMed:21441914, PubMed:22102415). Homodimerization facilitates DNA binding (PubMed:18854158).
4 PublicationsManual assertion based on experiment ini
- Ref.4"ATP hydrolysis by RAD50 protein switches MRE11 enzyme from endonuclease to exonuclease."
Majka J., Alford B., Ausio J., Finn R.M., McMurray C.T.
J. Biol. Chem. 287:2328-2341(2012) [PubMed] [Europe PMC] [Abstract]Cited for: ACTIVITY REGULATION, SUBUNIT. - Ref.6"Structural biochemistry and interaction architecture of the DNA double-strand break repair Mre11 nuclease and Rad50-ATPase."
Hopfner K.-P., Karcher A., Craig L., Woo T.T., Carney J.P., Tainer J.A.
Cell 105:473-485(2001) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-333 IN COMPLEX WITH MANGANESE, COFACTOR, SUBUNIT, ACTIVE SITE. - Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97. - Ref.9"ABC ATPase signature helices in Rad50 link nucleotide state to Mre11 interface for DNA repair."
Williams G.J., Williams R.S., Williams J.S., Moncalian G., Arvai A.S., Limbo O., Guenther G., SilDas S., Hammel M., Russell P., Tainer J.A.
Nat. Struct. Mol. Biol. 18:423-431(2011) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 348-381, SUBUNIT.
<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi
Show more detailsHide detailsQ8U1N9
| With | #Exp. | IntAct |
|---|---|---|
| itself | 3 | EBI-2014945,EBI-2014945 |
| rad50 [P58301] | 11 | EBI-2014945,EBI-2505704 |
GO - Molecular functioni
- identical protein binding Source: IntActInferred from physical interactioni
- Ref.8"Mre11 dimers coordinate DNA end bridging and nuclease processing in double-strand-break repair."
Williams R.S., Moncalian G., Williams J.S., Yamada Y., Limbo O., Shin D.S., Groocock L.M., Cahill D., Hitomi C., Guenther G., Moiani D., Carney J.P., Russell P., Tainer J.A.
Cell 135:97-109(2008) [PubMed] [Europe PMC] [Abstract]Cited for: X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) OF 1-343 IN COMPLEX WITH MANGANESE, FUNCTION, DNA-BINDING, COFACTOR, SUBUNIT, MUTAGENESIS OF HIS-17; HIS-52; LEU-61; HIS-85 AND LEU-97. - "The Mre11:Rad50 structure shows an ATP-dependent molecular clamp in DNA double-strand break repair."
Lammens K., Bemeleit D.J., Mockel C., Clausing E., Schele A., Hartung S., Schiller C.B., Lucas M., Angermuller C., Soding J., Strasser K., Hopfner K.P.
Cell 145:54-66(2011) [PubMed] [Europe PMC] [Abstract]
Protein-protein interaction databases
Database of interacting proteins More...DIPi | DIP-52386N |
Protein interaction database and analysis system More...IntActi | Q8U1N9, 1 interactor |
Molecular INTeraction database More...MINTi | Q8U1N9 |
STRING: functional protein association networks More...STRINGi | 186497.PF1166 |
<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more detailsHide details| Feature key | Position(s) | DescriptionActions | Graphical view | Length |
|---|---|---|---|---|
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined beta strands within the protein sequence.<p><a href='/help/strand' target='_top'>More...</a></p>Beta strandi | 2 – 6 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined helical regions within the protein sequence.<p><a href='/help/helix' target='_top'>More...</a></p>Helixi | 15 – 17 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 19 – 38 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 20 | |
| Beta strandi | 42 – 48 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 50 – 55 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 58 – 72 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 15 | |
| <p>This subsection of the <a href="http://www.uniprot.org/help/structure%5Fsection">'Structure'</a> section is used to indicate the positions of experimentally determined hydrogen-bonded turns within the protein sequence. These elements correspond to the DSSP secondary structure code 'T'.<p><a href='/help/turn' target='_top'>More...</a></p>Turni | 73 – 75 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 78 – 81 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 4 | |
| Turni | 84 – 86 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 89 – 91 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 94 – 100 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 108 – 112 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 116 – 123 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 129 – 135 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 138 – 143 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Helixi | 148 – 152 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 157 – 161 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 166 – 173 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 177 – 181 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Turni | 182 – 184 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Helixi | 192 – 194 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 200 – 206 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 | |
| Beta strandi | 211 – 215 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Beta strandi | 218 – 222 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 5 | |
| Helixi | 231 – 233 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 235 – 240 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 242 – 249 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Beta strandi | 254 – 259 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 262 – 267 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 273 – 280 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 282 – 292 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 11 | |
| Helixi | 293 – 295 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 3 | |
| Beta strandi | 301 – 310 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 10 | |
| Helixi | 315 – 320 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 6 | |
| Beta strandi | 324 – 332 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 9 | |
| Helixi | 354 – 361 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 8 | |
| Helixi | 370 – 376 | Combined sources Manual assertion inferred from combination of experimental and computational evidencei | 7 |
3D structure databases
SWISS-MODEL Repository - a database of annotated 3D protein structure models More...SMRi | Q8U1N9 |
Database of comparative protein structure models More...ModBasei | Search... |
Protein Data Bank in Europe - Knowledge Base More...PDBe-KBi | Search... |
Miscellaneous databases
Relative evolutionary importance of amino acids within a protein sequence More...EvolutionaryTracei | Q8U1N9 |
<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi
<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi
Phylogenomic databases
evolutionary genealogy of genes: Non-supervised Orthologous Groups More...eggNOGi | arCOG00397, Archaea |
The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms More...HOGENOMi | CLU_026621_5_1_2 |
Identification of Orthologs from Complete Genome Data More...OMAi | RWDFGDY |
Family and domain databases
Conserved Domains Database More...CDDi | cd00840, MPP_Mre11_N, 1 hit |
Gene3D Structural and Functional Annotation of Protein Families More...Gene3Di | 3.60.21.10, 1 hit |
HAMAP database of protein families More...HAMAPi | MF_02044, Mre11, 1 hit |
Integrated resource of protein families, domains and functional sites More...InterProi | View protein in InterPro IPR004843, Calcineurin-like_PHP_ApaH IPR029052, Metallo-depent_PP-like IPR032885, Mre11_archaea-type IPR041796, Mre11_N |
Pfam protein domain database More...Pfami | View protein in Pfam PF00149, Metallophos, 1 hit |
<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei
<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.
Q8U1N9-1 [UniParc]FASTAAdd to basketAdded to basket
« Hide
Show »10 20 30 40 50
MKFAHLADIH LGYEQFHKPQ REEEFAEAFK NALEIAVQEN VDFILIAGDL
60 70 80 90 100
FHSSRPSPGT LKKAIALLQI PKEHSIPVFA IEGNHDRTQR GPSVLNLLED
110 120 130 140 150
FGLVYVIGMR KEKVENEYLT SERLGNGEYL VKGVYKDLEI HGMKYMSSAW
160 170 180 190 200
FEANKEILKR LFRPTDNAIL MLHQGVREVS EARGEDYFEI GLGDLPEGYL
210 220 230 240 250
YYALGHIHKR YETSYSGSPV VYPGSLERWD FGDYEVRYEW DGIKFKERYG
260 270 280 290 300
VNKGFYIVED FKPRFVEIKV RPFIDVKIKG SEEEIRKAIK RLIPLIPKNA
310 320 330 340 350
YVRLNIGWRK PFDLTEIKEL LNVEYLKIDT WRIKERTDEE SGKIGLPSDF
360 370 380 390 400
FTEFELKIID ILGEKDFDDF DYIIKLITEG KVEEEGPLEE AVKKVSEEKG
410 420
KTVRQKIESI PKKKRGTLDS WLGGAR
Length:426
Mass (Da):49,456
Last modified:June 21, 2004 - v2
<p>The checksum is a form of redundancy check that is calculated
from the sequence. It is useful for tracking sequence updates.</p>
<p>It should be noted that while, in theory, two different sequences could
have the same checksum value, the likelihood that this would happen
is extremely low.</p>
<p>However UniProtKB may contain entries with identical sequences in case
of multiple genes (paralogs).</p>
<p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64)
using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1.
The algorithm is described in the ISO 3309 standard.
</p>
<p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br />
<strong>Cyclic redundancy and other checksums</strong><br />
<a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p>
Checksum:i639092C2F9C24DCD
<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni
The sequence AAL81290 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated
Sequence databases
| Select the link destinations: EMBL nucleotide sequence database More...EMBLiGenBank nucleotide sequence database More...GenBankiDNA Data Bank of Japan; a nucleotide sequence database More...DDBJiLinks Updated | AE009950 Genomic DNA Translation: AAL81290.1 Different initiation. |
Genome annotation databases
Ensembl bacterial and archaeal genome annotation project More...EnsemblBacteriai | AAL81290; AAL81290; PF1166 |
KEGG: Kyoto Encyclopedia of Genes and Genomes More...KEGGi | pfu:PF1166 |
Pathosystems Resource Integration Center (PATRIC) More...PATRICi | fig|186497.12.peg.1226 |
<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8U1N9 | DNA double-strand break repair protein Mre11 | 428 | UniRef90_Q8U1N9 | |||
| DNA double-strand break repair protein Mre11 | 428 | |||||
| +3 | ||||||
| Protein | Similar proteins | Species | Score | Length | Source | |
|---|---|---|---|---|---|---|
| Q8U1N9 | DNA double-strand break repair protein Mre11 | 413 | UniRef50_Q8U1N9 | |||
| DNA double-strand break repair protein Mre11 | 415 | |||||
| DNA double-strand break repair protein Mre11 | 428 | |||||
| DNA double-strand break repair protein Mre11 | 428 | |||||
| DNA double-strand break repair protein Mre11 | 414 | |||||
| +47 | ||||||
<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi
Sequence databases
| Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AE009950 Genomic DNA Translation: AAL81290.1 Different initiation. |
3D structure databases
| Select the link destinations: Protein Data Bank Europe More...PDBeiProtein Data Bank RCSB More...RCSB PDBiProtein Data Bank Japan More...PDBjiLinks Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
| 1II7 | X-ray | 2.20 | A/B | 1-333 | [»] | |
| 1S8E | X-ray | 2.30 | A/B | 1-333 | [»] | |
| 3DSC | X-ray | 2.70 | A | 1-343 | [»] | |
| 3DSD | X-ray | 2.20 | A/B | 1-343 | [»] | |
| 3QKR | X-ray | 3.40 | C | 348-381 | [»] | |
| 3QKS | X-ray | 2.10 | C | 348-381 | [»] | |
| 3QKU | X-ray | 3.30 | C | 348-381 | [»] | |
| 4HD0 | X-ray | 2.30 | A/B | 1-333 | [»] | |
| SMRi | Q8U1N9 | |||||
| ModBasei | Search... | |||||
| PDBe-KBi | Search... | |||||
Protein-protein interaction databases
| DIPi | DIP-52386N |
| IntActi | Q8U1N9, 1 interactor |
| MINTi | Q8U1N9 |
| STRINGi | 186497.PF1166 |
Genome annotation databases
| EnsemblBacteriai | AAL81290; AAL81290; PF1166 |
| KEGGi | pfu:PF1166 |
| PATRICi | fig|186497.12.peg.1226 |
Phylogenomic databases
| eggNOGi | arCOG00397, Archaea |
| HOGENOMi | CLU_026621_5_1_2 |
| OMAi | RWDFGDY |
Miscellaneous databases
| EvolutionaryTracei | Q8U1N9 |
Family and domain databases
| CDDi | cd00840, MPP_Mre11_N, 1 hit |
| Gene3Di | 3.60.21.10, 1 hit |
| HAMAPi | MF_02044, Mre11, 1 hit |
| InterProi | View protein in InterPro IPR004843, Calcineurin-like_PHP_ApaH IPR029052, Metallo-depent_PP-like IPR032885, Mre11_archaea-type IPR041796, Mre11_N |
| Pfami | View protein in Pfam PF00149, Metallophos, 1 hit |
ProtoNet; Automatic hierarchical classification of proteins More...ProtoNeti | Search... |
MobiDB: a database of protein disorder and mobility annotations More...MobiDBi | Search... |
<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi
| <p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry namei | MRE11_PYRFU | |
| <p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>Accessioni | Q8U1N9Primary (citable) accession number: Q8U1N9 | |
| <p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyi | Integrated into UniProtKB/Swiss-Prot: | June 21, 2004 |
| Last sequence update: | June 21, 2004 | |
| Last modified: | April 7, 2021 | |
| This is version 123 of the entry and version 2 of the sequence. See complete history. | ||
| <p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
| Annotation program | Prokaryotic Protein Annotation Program | |
<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi
Keywords - Technical termi
3D-structure, Reference proteomeDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families
